Failure of Viral Protein 3 of Infectious Bursal Disease Virus Produced in Prokaryotic and Eukaryotic Expression Systems to Protect Chickens against the Disease
Autor: | Krispel S, Di-Castro D, A Safadi, Pitcovski J, Aviva Azriel, Maray T, Amnon Michael, Ben-Zion Levi, B. Gutter |
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Rok vydání: | 1999 |
Předmět: |
animal structures
Viral protein viruses Blotting Western Virulence medicine.disease_cause Infectious bursal disease virus Virus law.invention Infectious bursal disease Capsid Food Animals law medicine Animals Escherichia coli Poultry Diseases Viral Structural Proteins General Immunology and Microbiology biology Viral Vaccine Viral Vaccines Birnaviridae Infections medicine.disease Virology Recombinant DNA biology.protein RNA Viral Capsid Proteins Electrophoresis Polyacrylamide Gel Animal Science and Zoology Antibody Chickens |
Zdroj: | Avian Diseases. 43:8 |
ISSN: | 0005-2086 |
DOI: | 10.2307/1592756 |
Popis: | In recent years, infectious bursal disease virus (IBDV) has become a serious economic problem as a result of the emergence of new and very virulent strains. Most of the antibodies produced against IBDV are for the structural proteins viral protein (VP) 2 (VP2) and VP3. The purpose of this study was to test the potential of recombinant VP3 to induce protective antibodies. The gene for VP3 was isolated from a virulent strain of the virus and cloned into prokaryotic (Escherichia coli) and eukaryotic (baculovirus) expression systems. The protein expressed by both systems was of the expected size (32 kD) and was detected by anti-IBDV antibodies. Following partial purification, the polypeptides were injected into intact birds and induced the production of high levels of anti-IBDV antibodies, as detected by immunoblot and enzyme-linked immunosorbent assay tests. These antibodies did not prevent changes in the bursa and mortality when birds were challenged with a virulent IBDV strain after vaccination with the recombinant VP3. The results show that VP3 polypeptide cannot be used as a subunit vaccine against IBDV and raise questions concerning the nature of the neutralizing epitope on this structural protein. |
Databáze: | OpenAIRE |
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